메뉴 건너뛰기




Volumn 382, Issue 1, 2004, Pages 323-329

Dual regulation of AP-2α transcriptional activation by poly(ADP-ribose) polymerase-1

Author keywords

Activator protein 2 ; Co activator; Poly(ADP ribose) polymerase 1; Post translational modification; Transcriptional regulation

Indexed keywords

BREAST CANCER; ENZYMIC ACTIVITY; POLYMERASE;

EID: 4344625329     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040593     Document Type: Article
Times cited : (28)

References (32)
  • 1
    • 0036733355 scopus 로고    scopus 로고
    • The therapeutic potential of poly(ADP-ribose) polymerase inhibitors
    • Virag, L. and Szabo, C. (2002) The therapeutic potential of poly(ADP-ribose) polymerase inhibitors. Pharmacol. Rev. 54, 375-429
    • (2002) Pharmacol. Rev. , vol.54 , pp. 375-429
    • Virag, L.1    Szabo, C.2
  • 2
    • 0031844678 scopus 로고    scopus 로고
    • Involvement of TFIID and USA components in transcriptional activation of the human immunodeficiency virus promoter by NF-κB and Sp1
    • Guermah, M., Malik, S. and Roeder, R. G. (1998) Involvement of TFIID and USA components in transcriptional activation of the human immunodeficiency virus promoter by NF-κB and Sp1. Mol. Cell. Biol. 18, 3234-3244
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3234-3244
    • Guermah, M.1    Malik, S.2    Roeder, R.G.3
  • 4
    • 0033953753 scopus 로고    scopus 로고
    • Identification of poly(ADP-ribose) polymerase as a transcriptional coactivator of the human T-cell leukemia virus type 1 Tax protein
    • Anderson, M. G., Scoggin, K. E., Simbulan-Rosenthal, C. M. and Steadman, J. A. (2000) Identification of poly(ADP-ribose) polymerase as a transcriptional coactivator of the human T-cell leukemia virus type 1 Tax protein. J. Virol. 74, 2169-2177
    • (2000) J. Virol. , vol.74 , pp. 2169-2177
    • Anderson, M.G.1    Scoggin, K.E.2    Simbulan-Rosenthal, C.M.3    Steadman, J.A.4
  • 5
    • 0032959888 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase binds with transcription enhancer factor 1 to MCAT1 elements to regulate muscle-specific transcription
    • Butler, A. J. and Ordahl, C. P. (1999) Poly(ADP-ribose) polymerase binds with transcription enhancer factor 1 to MCAT1 elements to regulate muscle-specific transcription. Mol. Cell. Biol. 19, 296-306
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 296-306
    • Butler, A.J.1    Ordahl, C.P.2
  • 6
    • 0344258423 scopus 로고    scopus 로고
    • PolyADP-ribose polymerase is a coactivator for AP-2-mediated transcriptional activation
    • Kannan, P., Yu, Y., Wankhade, S. and Tainsky, M. A. (1999) PolyADP-ribose polymerase is a coactivator for AP-2-mediated transcriptional activation. Nucleic Acids Res. 27, 866-874
    • (1999) Nucleic Acids Res. , vol.27 , pp. 866-874
    • Kannan, P.1    Yu, Y.2    Wankhade, S.3    Tainsky, M.A.4
  • 7
    • 0034615948 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase is a B-MYB coactivator
    • Cervellera, M. N. and Sala, A. (2000) Poly(ADP-ribose) polymerase is a B-MYB coactivator. J. Biol. Chem. 275, 10692-10696
    • (2000) J. Biol. Chem. , vol.275 , pp. 10692-10696
    • Cervellera, M.N.1    Sala, A.2
  • 8
    • 0345628001 scopus 로고    scopus 로고
    • Inhibitors of ADP-ribosylation impair inducible nitric oxide synthase gene transcription through inhibition of NF-κB activation
    • Le Page, C., Sanceau, J., Drapier, J. C. and Wietzerbin, J. (1998) Inhibitors of ADP-ribosylation impair inducible nitric oxide synthase gene transcription through inhibition of NF-κB activation. Biochem. Biophys. Res. Commun. 243, 451-457
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 451-457
    • Le Page, C.1    Sanceau, J.2    Drapier, J.C.3    Wietzerbin, J.4
  • 9
    • 0029099358 scopus 로고
    • Involvement of NAD-poly(ADP-ribose) metabolism in p53 regulation and its consequences
    • Whitacre, C. M., Hashimoto, H., Tsai, M. L., Chatterjee, S., Berger, S. J. and Berger, N. A. (1995) Involvement of NAD-poly(ADP-ribose) metabolism in p53 regulation and its consequences. Cancer Res. 55, 3697-3701
    • (1995) Cancer Res. , vol.55 , pp. 3697-3701
    • Whitacre, C.M.1    Hashimoto, H.2    Tsai, M.L.3    Chatterjee, S.4    Berger, S.J.5    Berger, N.A.6
  • 11
    • 0036710459 scopus 로고    scopus 로고
    • The functional role of poly(ADP-ribose)polymerase 1 as novel coactivator of NF-κB in inflammatory disorders
    • Hassa, P. O. and Hottiger, M. O. (2002) The functional role of poly(ADP-ribose)polymerase 1 as novel coactivator of NF-κB in inflammatory disorders. Cell. Mol. Life Sci. 59, 1534-1553
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1534-1553
    • Hassa, P.O.1    Hottiger, M.O.2
  • 12
    • 0038682011 scopus 로고    scopus 로고
    • PARP goes transcription
    • Cambridge, Mass.
    • Kraus, W. L. and Lis, J. T. (2003) PARP goes transcription. Cell (Cambridge, Mass.) 113, 677-683
    • (2003) Cell , vol.113 , pp. 677-683
    • Kraus, W.L.1    Lis, J.T.2
  • 13
    • 0028352111 scopus 로고
    • N-ras oncogene causes AP-2 transcriptional self-interference, which leads to transformation
    • Kannan, P., Buettner, R., Chiao, P. J., Yim, S. O., Sarkiss, M. and Tainsky, M. A. (1994) N-ras oncogene causes AP-2 transcriptional self-interference, which leads to transformation. Genes Dev. 8, 1258-1269
    • (1994) Genes Dev. , vol.8 , pp. 1258-1269
    • Kannan, P.1    Buettner, R.2    Chiao, P.J.3    Yim, S.O.4    Sarkiss, M.5    Tainsky, M.A.6
  • 14
    • 0037160111 scopus 로고    scopus 로고
    • Tumor suppressor activity of AP2α mediated through a direct interaction with p53
    • McPherson, L. A., Loktev, A. V. and Weigel, R. J. (2002) Tumor suppressor activity of AP2α mediated through a direct interaction with p53. J. Biol. Chem. 277, 45028-45033
    • (2002) J. Biol. Chem. , vol.277 , pp. 45028-45033
    • McPherson, L.A.1    Loktev, A.V.2    Weigel, R.J.3
  • 15
    • 0346101795 scopus 로고    scopus 로고
    • Cell cycle arrest and apoptosis induction by activator protein 2α (NP-Zα) and the role of p53 and p21WAF1/CIP1 in AP-2α mediated growth inhibition
    • Wajapeyee, N. and Somasundaram, K. (2003) Cell cycle arrest and apoptosis induction by activator protein 2α (NP-Zα) and the role of p53 and p21WAF1/CIP1 in AP-2α mediated growth inhibition. J. Biol. Chem. 278, 52093-52101
    • (2003) J. Biol. Chem. , vol.278 , pp. 52093-52101
    • Wajapeyee, N.1    Somasundaram, K.2
  • 16
    • 0037073377 scopus 로고    scopus 로고
    • The human transcription factor activation protein-2γ (AP-2γ): Gene structure, promoter, and expression in mammary carcinoma cell lines
    • Li, M., Wang, Y., Yu, Y., Nishizawa, M., Nakajima, T., Ito, S. and Kannan, P. (2002) The human transcription factor activation protein-2γ (AP-2γ): gene structure, promoter, and expression in mammary carcinoma cell lines. Gene 301, 43-51
    • (2002) Gene , vol.301 , pp. 43-51
    • Li, M.1    Wang, Y.2    Yu, Y.3    Nishizawa, M.4    Nakajima, T.5    Ito, S.6    Kannan, P.7
  • 17
    • 0034731455 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins
    • Pleschke, J. M., Kleczkowska, H. E., Strohm, M. and Althaus, F. R. (2000) Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J. Biol. Chem. 275, 40974-40980
    • (2000) J. Biol. Chem. , vol.275 , pp. 40974-40980
    • Pleschke, J.M.1    Kleczkowska, H.E.2    Strohm, M.3    Althaus, F.R.4
  • 18
    • 0343852709 scopus 로고    scopus 로고
    • Protein-protein interaction of the human poly(ADP-ribosyl)transferase depends on the functional state of the enzyme
    • Griesenbeck, J., Oei, S. L., Mayer-Kuckuk, P., Ziegler, M., Buchlow, G. and Schweiger, M. (1997) Protein-protein interaction of the human poly(ADP-ribosyl)transferase depends on the functional state of the enzyme. Biochemistry 36, 7297-7304
    • (1997) Biochemistry , vol.36 , pp. 7297-7304
    • Griesenbeck, J.1    Oei, S.L.2    Mayer-Kuckuk, P.3    Ziegler, M.4    Buchlow, G.5    Schweiger, M.6
  • 19
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D. B. and Johnson, K. S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67, 31-40
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 20
    • 0026506694 scopus 로고
    • Noncovalent interactions of poly(adenosine diphosphate ribose) with histones
    • Panzeter, P. L., Realini, C. A. and Althaus, F. R. (1992) Noncovalent interactions of poly(adenosine diphosphate ribose) with histones. Biochemistry 31, 1379-1385
    • (1992) Biochemistry , vol.31 , pp. 1379-1385
    • Panzeter, P.L.1    Realini, C.A.2    Althaus, F.R.3
  • 22
    • 0032533856 scopus 로고    scopus 로고
    • Functional interactions of p53 with poly(ADP-ribose) polymerase (PARP) during apoptosis following DNA damage: Covalent poly(ADP-ribosyl)ation of p53 by exogenous PARP and noncovalent binding of p53 to the M(r) 85 000 proteolytic fragment
    • Kumari, S. R., Mendoza-Alvarez, H. and Alvarez-Gonzalez, R. (1998) Functional interactions of p53 with poly(ADP-ribose) polymerase (PARP) during apoptosis following DNA damage: covalent poly(ADP-ribosyl)ation of p53 by exogenous PARP and noncovalent binding of p53 to the M(r) 85 000 proteolytic fragment. Cancer Res. 58, 5075-5078
    • (1998) Cancer Res. , vol.58 , pp. 5075-5078
    • Kumari, S.R.1    Mendoza-Alvarez, H.2    Alvarez-Gonzalez, R.3
  • 23
    • 0032496235 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains of p53 and alters its DNA binding functions
    • Malanga, M., Pleschke, J. M., Kleczkowska, H. E. and Althaus, F. R. (1998) Poly(ADP-ribose) binds to specific domains of p53 and alters its DNA binding functions. J. Biol. Chem. 273, 11839-11843
    • (1998) J. Biol. Chem. , vol.273 , pp. 11839-11843
    • Malanga, M.1    Pleschke, J.M.2    Kleczkowska, H.E.3    Althaus, F.R.4
  • 24
    • 0034703026 scopus 로고    scopus 로고
    • Characterization of the activation domains of AP-2 family transcription factors
    • Wankhade, S., Yu, Y., Weinberg, J., Tainsky, M. A. and Kannan, P. (2000) Characterization of the activation domains of AP-2 family transcription factors. J. Biol. Chem. 275, 29701-29708
    • (2000) J. Biol. Chem. , vol.275 , pp. 29701-29708
    • Wankhade, S.1    Yu, Y.2    Weinberg, J.3    Tainsky, M.A.4    Kannan, P.5
  • 25
    • 0036327370 scopus 로고    scopus 로고
    • Tumorigenic effect of transcription factor hAP-2α and the intricate link between hAP-2α activation and squelching
    • Yu, Y., Wang, Y., Li, M. and Kannan, P. (2002) Tumorigenic effect of transcription factor hAP-2α and the intricate link between hAP-2α activation and squelching. Mol. Carcinog. 34, 172-179
    • (2002) Mol. Carcinog. , vol.34 , pp. 172-179
    • Yu, Y.1    Wang, Y.2    Li, M.3    Kannan, P.4
  • 26
    • 0031031787 scopus 로고    scopus 로고
    • From BRCA1 to RAP1: A widespread BRCT module closely associated with DNA repair
    • Callebaut, I. and Mornon, J. P. (1997) From BRCA1 to RAP1: a widespread BRCT module closely associated with DNA repair. FEBS Lett. 400, 25-30
    • (1997) FEBS Lett. , vol.400 , pp. 25-30
    • Callebaut, I.1    Mornon, J.P.2
  • 28
    • 0035824647 scopus 로고    scopus 로고
    • The enzymatic and DNA binding activity of PARP-1 are not required for NF-κB coactivator function. J
    • Hassa, P. O., Covic, M., Hasan, S., Imhof, R. and Hottiger, M. O. (2001) The enzymatic and DNA binding activity of PARP-1 are not required for NF-κB coactivator function. J. Biol. Chem. 276, 45588-45597
    • (2001) Biol. Chem. , vol.276 , pp. 45588-45597
    • Hassa, P.O.1    Covic, M.2    Hasan, S.3    Imhof, R.4    Hottiger, M.O.5
  • 29
    • 0032501965 scopus 로고    scopus 로고
    • A novel function of poly(ADP-ribosyl)ation: Silencing of RNA polymerase II-dependent transcription
    • Oei, S. L., Griesenbeck, J., Ziegler, M. and Schweiger, M. (1998) A novel function of poly(ADP-ribosyl)ation: silencing of RNA polymerase II-dependent transcription. Biochemistry 37, 1465-1469
    • (1998) Biochemistry , vol.37 , pp. 1465-1469
    • Oei, S.L.1    Griesenbeck, J.2    Ziegler, M.3    Schweiger, M.4
  • 30
    • 0037462597 scopus 로고    scopus 로고
    • Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci
    • Tulin, A. and Spradling, A. (2003) Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci. Science 299, 560-562
    • (2003) Science , vol.299 , pp. 560-562
    • Tulin, A.1    Spradling, A.2
  • 31
    • 0035425899 scopus 로고    scopus 로고
    • Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism
    • Davidovic, L., Vodenicharov, M., Affar, E. B. and Poirier, G. G. (2001) Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism. Exp. Cell Res. 268, 7-13
    • (2001) Exp. Cell Res. , vol.268 , pp. 7-13
    • Davidovic, L.1    Vodenicharov, M.2    Affar, E.B.3    Poirier, G.G.4
  • 32
    • 0024428970 scopus 로고
    • Poly(ADP-ribose) catabolism in mammalian cells exposed to DNA-damaging agents
    • Alvarez-Gonzalez, R. and Althaus, F. R. (1989) Poly(ADP-ribose) catabolism in mammalian cells exposed to DNA-damaging agents. Mutat. Res. 218, 67-74
    • (1989) Mutat. Res. , vol.218 , pp. 67-74
    • Alvarez-Gonzalez, R.1    Althaus, F.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.